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9 November 2018 Cloning and Expression Profile of Glyceraldehyde-3Phosphate Dehydrogenase in Haemaphysalis flava (Acari: Ixodidae)
Lv Xu, Lei Liu, Tian-yin Cheng
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Haemaphysalis flava (Acari: Ixodidae) harbors pathogenic microorganisms and transfers these to hosts during blood feeding. Proteomic analysis in the midgut contents of H. flava detected glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and contig 1683 was retrieved as a GAPDH gene fragment by searching our previous transcriptomic library. In the study, the 5′ and 3′ ends of contig 1683 were cloned by rapid amplification of cDNA ends (RACE) and a full length, 1340 bp cDNA of Hf-GAPDH was obtained. The open-reading frame had 999 bp and coded for 333 amino acids. Hf-GAPDH was predicted to have an N-terminal NAD binding domain and a C-terminal glyceraldehyde dehydrogenase catalytic domain. The molecular structure of Hf-GAPDH was analyzed and the evolutionary relationship also established. The GAPDH protein sequence was conserved among ticks. The expression pattern of Hf-GAPDH, analyzed by real-time PCR, significantly differed among life phases, feeding stages, and tissues. As the ticks grew, the expression level of Hf-GAPDH was up-regulated. The expression levels of Hf-GAPDH in salivary glands and midguts from half-engorged ticks were lower than the same tissues from engorged ticks. This study will provide reference data for the follow-up verification of the GAPDH-related function and the feasibility as a potential anti-tick vaccine.

© The Author(s) 2018. Published by Oxford University Press on behalf of Entomological Society of America. All rights reserved. For permissions, please e-mail:
Lv Xu, Lei Liu, and Tian-yin Cheng "Cloning and Expression Profile of Glyceraldehyde-3Phosphate Dehydrogenase in Haemaphysalis flava (Acari: Ixodidae)," Journal of Medical Entomology 56(2), 569-575, (9 November 2018).
Received: 23 July 2018; Accepted: 15 October 2018; Published: 9 November 2018

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real-time PCR
salivary gland
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